Characterization of monoclonal antibodies specific for the pre-S2 region of the hepatitis B virus envelope protein

1986 ◽  
Vol 23 (9) ◽  
pp. 991-997 ◽  
Author(s):  
A.R. Neurath ◽  
P. Adamowicz ◽  
S.B.H. Kent ◽  
M.M. Riottot ◽  
N. Strick ◽  
...  
Author(s):  
Timothy M. Block ◽  
Xuanyong Lu ◽  
Anand Mehta ◽  
Jason Park ◽  
Baruch S. Blumberg ◽  
...  

2005 ◽  
Vol 79 (12) ◽  
pp. 7918-7921 ◽  
Author(s):  
Britta Kluge ◽  
Michaela Schläger ◽  
Alexander Pairan ◽  
Volker Bruss

ABSTRACT The cytosolic matrix domain (MD) located between amino acids (aa) 103 and 124 of the large hepatitis B virus envelope protein L is essential for virion formation. We reduced the distance between MD and the transmembrane domain (TD; aa 254 to 272) by deletions starting at aa 132. Six mutants with deletions of up to aa 234 were wild type, and four mutants with slightly larger deletions were blocked with respect to virion morphogenesis. Thus, the minimal distance between MD and TD was around 26 aa. This spacer might be required by MD to reach contact sites on the capsid.


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